๐”– Bobbio Scriptorium
โœฆ   LIBER   โœฆ

Control of the activity of intracellular nucleases in Neurospora crassa

โœ Scribed by Hasunuma, Kohji


Publisher
Springer
Year
1978
Tongue
English
Weight
638 KB
Volume
160
Category
Article
ISSN
0026-8925

No coin nor oath required. For personal study only.


๐Ÿ“œ SIMILAR VOLUMES


Method for identification of intracellul
โœ Lutz Scheideler; Helga Ninnemann ๐Ÿ“‚ Article ๐Ÿ“… 1988 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 400 KB

Establishing the relative intracellular proportions of flavins in Neurospora crassa (and in other organisms) in vivo may be hampered by degradation of flavins after homogenization of the cells. The system described here allows separation and identification of intracellular free and bound flavins und

Control of the production of orthophosph
โœ Hasunuma, Kohji ๐Ÿ“‚ Article ๐Ÿ“… 1977 ๐Ÿ› Springer ๐ŸŒ English โš– 522 KB

The abilities of purine- and pyrimidine-requiring mutants to produce six orthophosphate repressible extracellular enzymes, alkaline phosphatase, 5'-nucleotidase, acid phosphatase, two nucleases and ribonuclease N1 were examined by culturing these mutants in low and high phosphate media containing nu

Restricted activation of general amino a
โœ Kolanus, Johanna ;Michalczyk, Jens ;Flint, Harry J. ;Barthelmess, Ilse B. ๐Ÿ“‚ Article ๐Ÿ“… 1990 ๐Ÿ› Springer ๐ŸŒ English โš– 843 KB

In Neurospora crassa limitation for single amino acids normally results in increased formation of enzymes required for amino acid synthesis via 'general amino acid control'. Glutamine limitation, however, led to comparatively low and delayed derepression of enzyme synthesis. Nitrate reductase activi

Genetic and metabolic control of the pur
โœ Reinert, William R. ;Marzluf, George A. ๐Ÿ“‚ Article ๐Ÿ“… 1975 ๐Ÿ› Springer ๐ŸŒ English โš– 1008 KB

Neurospora crassa can utilize various purine bases such as xanthine or uric acid and their catabolic products as a nitrogen source. Four classes of mutants which affect the purine degradative pathway were isolated and studied. Mutants of the aln-1 class specifically lack allantoinase, while alc-1 mu